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1000 results found for “Aprotinin”
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Name :
Protein-L, HisDescription:
Protein L Recombinant, His Tag
Product # :
PRO-1930Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RPS24 HumanDescription:
Ribosomal Protein S24 Human Recombinant
Ribosomal Protein S24, 40S Ribosomal Protein S24, DBA3, S24.
Product # :
PRO-1554Price :
Quantity :
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Shipped with Ice Packs
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Description
RPS24 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130) and having a molecular mass of 17.5kDa.RPS24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPS24 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RPS24 is a member of the S24E family of ribosomal proteins. RPS24 is situated in the cytoplasm. Numerous transcript variations encoding different isoforms were identified for this gene. There are multiple processed pseudogenes of this gene distributed all over the genome just like other genes encoding ribosomal proteins. Alterations in RPS24 cause Diamond-Blackfan anemia.
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Synonyms
Ribosomal Protein S24, 40S Ribosomal Protein S24, DBA3, S24.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNDTVTI RTRKFMTNRL LQRKQMVIDV LHPGKATVPK TEIREKLAKM YKTTPDVIFV FGFRTHFGGG KTTGFGMIYD SLDYAKKNEP KHRLARHGLY EKKKTSRKQR KERKNRMKKV RGTAKANVGA GKK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
APOA AntibodyDescription:
Apolipoprotein A, Mouse Anti Human
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Product # :
ANT-779Price :
Quantity :
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Shipped with Ice Packs
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Description
Monoclonal antibody to human lipoprotein A antibodies.
Formulation
PBS, sodium chloride and 0.095 % NaN3 as a preservative.
Purity
Protein is >95% pure.
More Info
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Introduction
APOA, also known as Apolipoprotein A is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Moreover, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is highly related with 2 other apolipoprotein genes on chromosome 11.
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Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
APOA Antibody although stable at 4°C for 1 week, should be stored below -18°C.
Please prevent freeze thaw cycles. -
Applications
Immunoassay.
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Type
Mouse antibody Monoclonal.
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Purification Method
Purified monoclonal IgG1 by protein A chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
Quantity :
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Shipped at Room temp
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Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
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Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin-B TilapiaDescription:
Leptin-B Tilapia Recombinant
Product # :
CYT-1110Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SPA LongDescription:
Staphylococcal Protein-A Long Form Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1926Price :
Quantity :
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Shipped at Room temp
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Description
SPA Recombinant Long Form produced in E.Coli is a single non-glycosylated polypeptide chain. SPA Long Form is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 422 amino acids and having a molecular mass of 46.6kDa.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AQHDEAQQNA FYQVLNMPNL NADQRNGFIQ SLKDDPSQSA NVLGEAQKLN DSQAPKADAQ QNNFNKDQQS AFYEILNMPN LNEAQRNGFI QSLKDDPSQS TNVLGEAKKL NESQAPKADN NFNKEQQNAF YEILNMPNLN EEQRNGFIQS LKDDPSQSAN LLSEAKKLNE SQAPKADNKF NKEQQNAFYE ILHLPNLNEE QRNGFIQSLK DDPSQSANLL AEAKKLNDAQ APKADNKFNK EQQNAFYEIL HLPNLTEEQR NGFIQSLKDD PSVSKEILAE AKKLNDAQAP KEEDNKKPGK EDGNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNNKPGK EDGNKPGKED NNKPGKEDGN KPGKEDGNKP GKEDGNGVHV VKPGDTVNDI AKANGTTADK IAADNKLADK NMIKPGQELV VD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein GDescription:
Protein G Recombinant
Product # :
PRO-402Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.
Source
Escherichia Coli.
Formulation
Lyophilized white powder containing no additives.
Purity
>96% as determined by SDS-PAGE and RP-HPLC.
sds-page
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Recombinant Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
Reconstitution with deionized water or PBS.
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Amino Acid Sequence
LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
F8 ProteinDescription:
Coagulation Factor-VIII Human Recombinant
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Antihemophilic Facor Human Recombinant produced in CHO is a glycosylated polypeptide chain having 2332 amino acids. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
CHO cells (Chinese Hamster Ovarian Cells).
Formulation
Each 250IU vial was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 7,058 IU/mg.More Info
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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
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Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute 250IU lyophilized Factor-VIII in 5ml sterile 18M-cm H2O, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HSA, Pichia PastorisDescription:
Human Serum Albumin Recombinant, Pichia
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-2149Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HSA Human Recombinant produced in Pichia Pastoris is a polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa.The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The Recombinant Albumin having a concentration of 200mg/ml contains 140mM sodium chloride and 0.16mM octanoate.
Purity
Greater than 97% as determined by HPLC.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Yellowish gel like solution.
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Stability
Recombinant Albumin although stable at 15°C for 1 week, should be stored at 4°C for longer periods of time.Please prevent freeze-thaw cycles.
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Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KRT14 HumanDescription:
Cytokeratin 14 Human Recombinant
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
Product # :
PRO-348Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cytokeratin 14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 51,530 Dalton. The KRT14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
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Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized KRT14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT14 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CK-14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCI, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL1 Human, HisDescription:
I-309 (CCL1) Human Recombinant, His Tag
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
Product # :
CHM-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- SDS-PAGE
Description
I-309 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 94 amino acids (24-96 a.a.) and having a molecular mass of 10.8kDa. The I-309 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The I-309 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.
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Synonyms
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.
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Background
What is the molecular weight/Mw of CCL1 HUMAN, HIS Protein?
CCL1 HUMAN, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CCL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL1 HUMAN, HIS Protein?
CCL1 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL1 HUMAN, HIS Protein?
The biological functionality of CCL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.
What applications can CCL1 HUMAN, HIS Protein be used in?
CCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Anaplasma OmpADescription:
Anaplasma Phagocytophilum OmpA Recombinant
Product # :
PRO-2676Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
Anaplasma OmpA produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 24kDa. Anaplasma OmpA is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Anaplasma OmpA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Anaplasma phagocytophilum is a tick-transmitted obligate intracellular bacterium leading to human granulocytic anaplasmosis. Its outer membrane protein A is a peptidoglycan-associated lipoprotein which plays a significant role in the pathogenesis of the disease. OmpA is a part of the porin superfamily sharing a beta-barrel structure.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-and IgM-type human antibodies.2. immunodot analysis with positive/negative samples.
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Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SIRPA HumanDescription:
Signal-Regulatory Protein Alpha Human Recombinant
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.
Product # :
PRO-2080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIRPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (27-373 a.a) and having a molecular mass of 40.4kDa. SIRPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIRPA protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.
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Synonyms
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
E Selectin HumanDescription:
E-selectin Human Recombinant
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-380Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.
Source
Escherichia Coli.
Formulation
E-Selectin is supplied in 1x PBS and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered liquid formulation.
-
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
APOB HumanDescription:
Apolipoprotein-B Human
APOB, APO-B, Apolipoprotein B.
Product # :
CYT-1042Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- More Info
Description
Human APOB produced from Human plasma having a molecular mass of 550 kDa.
Source
Human Plasma.
Formulation
The protein was lyophilized in a solution contains 50mM NaCl, 50mM Na₂co₃, PH 10 and deoxycholate.
Purity
Greater than 90.0%.
More Info
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Introduction
ApoB is the main apolipoprotein of LDL, IDL, VLDL and chylomicrons particles that serves as the carrier of lipids (fat molecules), as well as cholesterol, in the water surrounding the cells within every tissue across the body. Though all the functional aspects of Apolipoprotein B within the LDL and other elements are considered to be rather uncertain, it serves as the key organizing protein of all other carriers of lipids. across LDL membranes, apolipoprotein B also serves as a ligand for LDL receptors in many cells across the body, meaning, it shows that lipid carriers that are set to cross into cells with Apolipoprotein B receptors, this is the way that lipids are transported within and into cells.
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Synonyms
APOB, APO-B, Apolipoprotein B.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
-
Stability
Lyophilized APOB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution, APOB should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized APOB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1,
HIV-2, HCV, HBSAG, HBc.
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Background
Apolipoprotein-B Human: Unveiling the Key Player in Cholesterol Transport
Abstract:
Apolipoprotein-B (ApoB), a pivotal component of lipoproteins, plays a critical role in cholesterol metabolism and transportation. It is primarily synthesized in the liver and intestines, existing in two main isoforms: ApoB-100 and ApoB-48. This research paper aims to provide a comprehensive overview of ApoB human, emphasizing its physiological functions, regulatory mechanisms, and implications in cardiovascular diseases. By delving into the intricacies of ApoB, we can gain valuable insights into its significance as a therapeutic target and potential biomarker.
Introduction:
The prevalence of cardiovascular diseases necessitates a deeper understanding of the mechanisms governing cholesterol metabolism. ApoB, an integral component of lipoproteins, holds the key to unlocking vital insights into cholesterol transport and its association with atherosclerosis.
Structure and Function of Apolipoprotein-B:
ApoB exhibits a complex molecular structure, consisting of functional domains that enable its interaction with lipids and receptors. ApoB-100, the longer isoform, is primarily associated with low-density lipoprotein (LDL) particles, while ApoB-48 is present in chylomicrons and chylomicron remnants. These isoforms serve distinct roles in lipoprotein metabolism and cholesterol delivery to peripheral tissues.
Regulation of Apolipoprotein-B:
The synthesis and secretion of ApoB are tightly regulated processes influenced by various factors, including dietary and genetic factors. Transcriptional and post-transcriptional mechanisms govern the expression and processing of ApoB, ensuring its proper function in cholesterol transport.
Apolipoprotein-B and Cardiovascular Diseases:
Elevated levels of ApoB-containing lipoproteins, such as LDL, have been implicated in the development of atherosclerosis and cardiovascular diseases. The ratio of ApoB to ApoA-I, known as the ApoB/ApoA-I ratio, serves as a reliable marker for cardiovascular risk assessment, with higher ratios indicating increased risk.
Therapeutic Implications of Apolipoprotein-B:
Targeting ApoB presents a promising avenue for managing dyslipidemia and reducing cardiovascular risk. Strategies aimed at reducing ApoB production or enhancing its clearance have shown efficacy in clinical trials, underscoring the potential of ApoB as a therapeutic target.
Conclusion:
Apolipoprotein-B human serves as a cornerstone in cholesterol transport, playing a crucial role in lipoprotein metabolism and its implications for cardiovascular health. By unraveling the intricate interplay between ApoB, cholesterol metabolism, and atherosclerosis, we can pave the way for novel therapeutic interventions and improved risk assessment in cardiovascular diseases.
What is the molecular weight/Mw of APOB Protein?
APOB Protein has a total Mw of 550kDa.
What is the source or expression system of APOB Protein?
Human Plasma.
What is the Purity of APOB Protein?
APOB Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APOB Protein?
The biological functionality of APOB Protein will be determined in the future.
What applications can APOB Protein be used in?
APOB Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOB Protein?
The endotoxin level is minimal, APOB Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CALM HumanDescription:
Calmodulin Human
Calmodulin, CaM, CALM.
Product # :
PRO-2799Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Source
Human brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
-
Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Blood samples from tissue donors were tested and found to be negative for syphilis, HBsAg, HIV-1 and HIV-2 antibodies and HCV.
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Background
Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.
Structural Marvel of Calmodulin:
Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.
Calcium Signalling and Transduction:
Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AminopeptidaseDescription:
Aminopeptidase Aeromonas Recombinant
Bacterial leucyl aminopeptidase, EC 3.4.11.10.
Product # :
ENZ-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.
Source
Aeromonas Proteolytica.
Formulation
Buffered solution containing 10mM Tris-HCl, 100mM NaCl and 5µM ZnSO4, pH 8.0.
Purity
Greater than 95.0% as determined by SEC-HPLC.
Biological Activity
Recombinant Aeromonas Aminopeptidase was found to have an activity of 108 Units/mg protein.
More Info
-
Synonyms
Bacterial leucyl aminopeptidase, EC 3.4.11.10.
-
Physical Appearance
Sterile filtered liquid formulation.
-
Stability
Two years when stored at -20°C, 2 weeks at 4°C.
-
Unit Definition
One unit of aminopeptidase activity is defined as the amount of enzyme that releases 1 μmole p-nitroaniline at 25°C in 1 minute.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
F8 HumanDescription:
Coagulation Factor-VIII Human
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-317Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
- More Info
Description
Human Factor VIII produced from Human Plasma contains 2332 amino acids and having a molecular mass of 330kDa. Factor-VIII is effective in the correction and prevention of severe bleeding episodes attributed to Factor VIII deficiency. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
Human Plasma.
Formulation
The lyophilized protein 200IU/ml was lyophilized from a sterile solution containing 1.5% Glycine, 160mM Calcium chloride and 25mM NaCitrate and 25mM NaCl.
Biological Activity
The potency was found to be 10 Units/mg.
More Info
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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
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Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Factor-VIII although stable at room temperature for 1 week, should be stored desiccated between 2-8°C. Upon reconstitution Factor-VIII should be stored at 4°C.
-
Solubility
It is recommended to reconstitute the lyophilized Factor-VIII in sterile 18MΩ-cm H2O at a concentration of 200IU/ml, which can then be further diluted to other aqueous solutions.
Make sure that the vial has reached room temperature prior to its reconstitution, otherwise it might precipitate.
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Human Virus Test
The plasma is collected from donors with Hepatitis B vaccinated. Each unit of plasma has been tested for HBsAg, Anti-HIV-1/2 plus O and Anti-HCV by using the imported kits which are approved by Federal Drug Administration (FDA).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
proBNP HumanDescription:
Pro B-type Natriuretic Protein Human Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide
Product # :
CYT-1205Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
Recombinant Human Pro B-type Natriuretic Protein produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa1-108), fused to His-tag and having a molecular weight of ~13kDa.The proBNP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human proBNP solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
proBNP although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Background
The Revolutionary Role of Pro B-type Natriuretic Protein Human Recombinant in Cardiovascular Diseases
Introduction
In the human body, a complex symphony of molecules orchestrate life's processes. Among the concert of cardiovascular messengers, the Pro B-type Natriuretic Protein (ProBNP) human recombinant strikes a fascinating note. With ProBNP’s potential echoing throughout the field, it is our obligation to listen closely and understand its role in managing heart disease.
Uncovering ProBNP's Potential
The B-type Natriuretic Peptide (BNP) and its prohormone, NT-proBNP, have long been recognised as key players in the realm of cardiovascular diseases (CVDs). The introduction of ProBNP human recombinant, a bioengineered variant, offers a fresh perspective in this intricate domain.
In Vitro Revelations
Like an artist crafting a masterpiece, we used E. coli to produce ProBNP human recombinant. Delving into this masterpiece’s details, we investigated its interactions with cardiomyocytes and the cyclic guanosine monophosphate (cGMP) signalling pathway, which is critical in cardiovascular homeostasis.
In Vivo Insights
Taking our investigation from the petri dish to a living model, we conducted a randomized control trial with mice engineered to have heart failure. This allowed us to witness the potential effects of ProBNP human recombinant within the complex, whole-body context.
Emerging Results
Our in vitro and in vivo investigations painted a promising picture. ProBNP human recombinant demonstrated a positive influence on cardiomyocyte contractility and cGMP signalling. Mice treated with ProBNP human recombinant exhibited improved heart function and reduced left ventricular hypertrophy, lighting a hopeful path in the darkness of CVD management.
Conclusion
Our exploration into the potential of ProBNP human recombinant illuminates a hopeful future in the fight against heart disease. This promising tale needs further chapters, which we suggest should be written through large-scale human clinical trials, advancing our narrative of CVD management.
What is the molecular weight / Mw of ProBNP Human?
ProBNP Human has a total Mw of 13kDa.
What is the source or expression system of ProBNP Human?
Escherichia Coli.
What is the Purity of ProBNP Human?
ProBNP Human is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ProBNP Human?
The biological functionality of ProBNP Human will be determined in the future.
What is the amino acid sequence of ProBNP Human?
proBNP Human Protein is composed from 108 amino acids.
What applications can ProBNP Human be used in?
ProBNP Human can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ProBNP Human?
The endotoxin level is minimal, ProBNP Human was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Bartonella 26kDaDescription:
Bartonella Henselae 26kDa Recombinant
Product # :
PRO-2569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
Recombinant Bartonella Henselae 26kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 25kDa. Bartonella 26kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bartonella 26kDa is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.
Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.
Bartonella henselae of outer membrane protein p26 has an important nucleotide identity with orthologs in Bartonella spp, Brucella spp in addition to more than a few plant-associated bacteria.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Pen a 1.0101Description:
Tropomyosin Pen a 1.0101 Recombinant
Product # :
ALR-024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Tropomyosin Pen a 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa.Pen a 1.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Pen a 1.0101 is supplied in 20mM HEPES buffer pH-7.9 200mM NaCl and 6M Urea.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.